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Conserved domains on  [gi|312233124|ref|YP_004021104|]
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cytochrome c oxidase subunit II (mitochondrion) [Solenopsis invicta]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 2.38e-122

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 346.43  E-value: 2.38e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   1 MNTWL-IALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPS 79
Cdd:MTH00154   1 MATWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  80 IKILYLTDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312233124 160 HAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMI 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 2.38e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 346.43  E-value: 2.38e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   1 MNTWL-IALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPS 79
Cdd:MTH00154   1 MATWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  80 IKILYLTDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312233124 160 HAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMI 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-221 1.03e-85

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 249.79  E-value: 1.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  94 LSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 173
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 312233124 174 TPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNW 221
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 9.61e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 219.20  E-value: 9.61e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   94 LSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 312233124  174 TPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
56-222 9.00e-44

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 146.51  E-value: 9.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  56 HGHSIELIWTILPMFILIFIAMPSIKILYLTDEIHNNKLSIKSIGHQWYWSYEYSDfpsiefdsfmipSDQLMDNEFRLl 135
Cdd:COG1622   75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIATVNELVL- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124 136 dvdnrcilPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNF 215
Cdd:COG1622  142 --------PVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                 ....*..
gi 312233124 216 PNFKNWL 222
Cdd:COG1622  214 EEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 56-211 1.78e-34

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 121.72  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   56 HGHSIELIWTILPMFILIFIAMPSI-KILYLTDEIHNNKLSIKSIGHQWYWSYEYSDFpsiefdsfmipsdqlmdnefrL 134
Cdd:TIGR02866  52 GNRRLEYVWTVIPLIIVVGLFAATAkGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------G 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312233124  135 LDVDNRCILPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVE 211
Cdd:TIGR02866 111 FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 2.38e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 346.43  E-value: 2.38e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   1 MNTWL-IALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPS 79
Cdd:MTH00154   1 MATWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  80 IKILYLTDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312233124 160 HAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMI 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 8-225 4.80e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 302.63  E-value: 4.80e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   8 LQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKILYLTD 87
Cdd:MTH00140   9 FQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  88 EIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLPSL 167
Cdd:MTH00140  89 ETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 312233124 168 GIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNM 225
Cdd:MTH00140 169 GVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-228 5.78e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 297.38  E-value: 5.78e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   1 MNTWL-IALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPS 79
Cdd:MTH00038   1 MATWLqLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  80 IKILYLTDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVI 159
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312233124 160 HAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMINN 228
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 3.11e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 292.65  E-value: 3.11e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   1 MNTWL-IALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPS 79
Cdd:MTH00168   1 MATYSqLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  80 IKILYLTDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVI 159
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312233124 160 HAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLN 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-225 8.42e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 289.31  E-value: 8.42e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   1 MNTW-LIALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPS 79
Cdd:MTH00139   1 MAYWgQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  80 IKILYLTDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVI 159
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312233124 160 HAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNM 225
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 8-225 1.07e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 289.12  E-value: 1.07e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   8 LQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKILYLTD 87
Cdd:MTH00117   9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  88 EIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLPSL 167
Cdd:MTH00117  89 EINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 312233124 168 GIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNM 225
Cdd:MTH00117 169 GVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 3-227 1.85e-93

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 273.55  E-value: 1.85e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   3 TWLIALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKI 82
Cdd:MTH00023  13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  83 LYLTDEIHNNKLSIKSIGHQWYWSYEYSDF--PSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIH 160
Cdd:MTH00023  93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312233124 161 AWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMIN 227
Cdd:MTH00023 173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 6-226 4.05e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 272.53  E-value: 4.05e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   6 IALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKILYL 85
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  86 TDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLP 165
Cdd:MTH00185  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312233124 166 SLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMI 226
Cdd:MTH00185 167 ALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 6-226 1.55e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 270.82  E-value: 1.55e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   6 IALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKILYL 85
Cdd:MTH00129   7 LGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  86 TDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLP 165
Cdd:MTH00129  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312233124 166 SLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMI 226
Cdd:MTH00129 167 ALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 6-224 5.16e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 269.80  E-value: 5.16e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   6 IALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKILYL 85
Cdd:MTH00008   7 LMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  86 TDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLP 165
Cdd:MTH00008  87 MDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 312233124 166 SLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLN 224
Cdd:MTH00008 167 SLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 8-226 2.13e-91

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 268.12  E-value: 2.13e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   8 LQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKILYLTD 87
Cdd:MTH00098   9 FQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  88 EIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLPSL 167
Cdd:MTH00098  89 EINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 312233124 168 GIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMI 226
Cdd:MTH00098 169 GLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-229 4.60e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 259.71  E-value: 4.60e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   4 WLIALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKIL 83
Cdd:MTH00051   7 WQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  84 YLTDEIHNNKLSIKSIGHQWYWSYEYSDFPS--IEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHA 161
Cdd:MTH00051  87 YLMDEVIDPALTIKAIGHQWYWSYEYSDYGTdtIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHS 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312233124 162 WTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMINNN 229
Cdd:MTH00051 167 FAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 6-227 6.44e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 259.33  E-value: 6.44e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   6 IALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKILYL 85
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  86 TDEIHNNKLSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLP 165
Cdd:MTH00076  87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312233124 166 SLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMIN 227
Cdd:MTH00076 167 SLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-221 1.03e-85

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 249.79  E-value: 1.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  94 LSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 173
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 312233124 174 TPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNW 221
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 9.61e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 219.20  E-value: 9.61e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   94 LSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 312233124  174 TPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVEST 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 16-227 1.08e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 223.35  E-value: 1.08e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  16 YDMMIFFHDFTMIILLFItililfiMILMINNKFINRYLLHGHSIELIWTILPMFILIFIAMPSIKILYLTdEIHN--NK 93
Cdd:MTH00080  26 NCSLLFGEFVLAFVVFLF-------LYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYY-GLMNldSN 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  94 LSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 173
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDA 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 312233124 174 TPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWLLNMIN 227
Cdd:MTH00080 178 MSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 9.95e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 206.80  E-value: 9.95e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   4 WLIALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMI-LMINNKFINRYL--LHGHSIELIWTILPMFILIFIAMPSI 80
Cdd:MTH00027  33 WQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  81 KILYLTDE-IHNNKLSIKSIGHQWYWSYEYSDF--PSIEFDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMD 157
Cdd:MTH00027 113 RLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAAD 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312233124 158 VIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWL 222
Cdd:MTH00027 193 VLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
56-222 9.00e-44

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 146.51  E-value: 9.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  56 HGHSIELIWTILPMFILIFIAMPSIKILYLTDEIHNNKLSIKSIGHQWYWSYEYSDfpsiefdsfmipSDQLMDNEFRLl 135
Cdd:COG1622   75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIATVNELVL- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124 136 dvdnrcilPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNF 215
Cdd:COG1622  142 --------PVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                 ....*..
gi 312233124 216 PNFKNWL 222
Cdd:COG1622  214 EEFDAWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 60-211 1.93e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 139.70  E-value: 1.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  60 IELIWTILPMFILIFIAmpSIKILYLTDEIHNN-KLSIKSIGHQWYWSYEYSDfpSIEFDSFMIPSDQLMDNEFRLLdvd 138
Cdd:MTH00047  49 LELLWTVVPTLLVLVLC--FLNLNFITSDLDCFsSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFGVDKPLRLV--- 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312233124 139 nrcilpFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVE 211
Cdd:MTH00047 122 ------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 56-211 1.78e-34

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 121.72  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124   56 HGHSIELIWTILPMFILIFIAMPSI-KILYLTDEIHNNKLSIKSIGHQWYWSYEYSDFpsiefdsfmipsdqlmdnefrL 134
Cdd:TIGR02866  52 GNRRLEYVWTVIPLIIVVGLFAATAkGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------G 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312233124  135 LDVDNRCILPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVE 211
Cdd:TIGR02866 111 FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-212 2.36e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 120.31  E-value: 2.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124 117 FDSFMIPSDQLMDNEFRLLDVDNRCILPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCS 196
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*.
gi 312233124 197 EICGINHSFMPIAVES 212
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEA 146
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-206 9.58e-25

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 93.84  E-value: 9.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  94 LSIKSIGHQWYWSYEYSDFPSIEFDSfmipsdqlmDNEFRLldvdnrcilPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 173
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGIVT---------ANELHI---------PVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 312233124 174 TPGRLNQTSMFINRPGIYFGQCSEICGINHSFM 206
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-211 2.23e-24

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 92.36  E-value: 2.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  94 LSIKSIGHQWYWSYEYSDfpSIEFDSFMIPSDQlmdnefrlldvdnrcilpfnfPIRILTTSMDVIHAWTLPSLGIKMDS 173
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN--VRTPNEIVVPAGT---------------------PVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 312233124 174 TPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVE 211
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-206 2.69e-19

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 79.60  E-value: 2.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  94 LSIKSIGHQWYWSYEYsdfpsiefdsfmiPSDQLMDNEfrlLDVdnrcilPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 173
Cdd:cd13915    2 LEIQVTGRQWMWEFTY-------------PNGKREINE---LHV------PVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 312233124 174 TPGRLNQTSMFINRPGIYFGQCSEICGINHSFM 206
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-206 2.51e-18

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 77.30  E-value: 2.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  94 LSIKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQLmdnefrlldvdnrcILPFNFPIRILTTSMDVIHAWTLPSLGIKMDS 173
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 312233124 174 TPGRLNQTSMFINRPGIYFGQCSEICGINHSFM 206
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 62-222 3.24e-18

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 77.88  E-value: 3.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  62 LIWTIlpmFILIFIAMPSikilyltDEIHNNKLSIKSIGHQWYWSYEYSDFPSiEFDSFMIPSDQlmdnefrlldvdnrc 141
Cdd:cd13918   11 IVWTY---GMLLYVEDPP-------DEADEDALEVEVEGFQFGWQFEYPNGVT-TGNTLRVPADT--------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124 142 ilpfnfPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNW 221
Cdd:cd13918   65 ------PIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138


                 .
gi 312233124 222 L 222
Cdd:cd13918  139 Y 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 6.51e-18

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 76.29  E-value: 6.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124  96 IKSIGHQWYWSYEYSDFPSIEFDSFMIPSDQlmdnefrlldvdnrcilpfnfPIRILTTSMDVIHAWTLPSLGIKMDSTP 175
Cdd:cd13914    3 IEVEAYQWGWEFSYPEANVTTSEQLVIPADR---------------------PVYFRITSRDVIHAFHVPELGLKQDAFP 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 312233124 176 GRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVESTNFPNFKNWL 222
Cdd:cd13914   62 GQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 4-82 5.51e-12

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 59.65  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312233124    4 WLIALQNSNSPIYDMMIFFHDFTMIILLFITILILFIMILMI------NNKFINRYLLHGHSIELIWTILPMFILIFIAM 77
Cdd:pfam02790   5 WGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILILIAL 84


                  ....*
gi 312233124   78 PSIKI 82
Cdd:pfam02790  85 PSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-206 8.26e-07

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 46.02  E-value: 8.26e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312233124 143 LPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFM 206
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 150-206 3.42e-04

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 38.51  E-value: 3.42e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 312233124 150 RILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFM 206
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 139-213 4.37e-04

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 38.30  E-value: 4.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312233124 139 NRCILPFNFPIRILTTSMDVIHAWTLPSLGIKMDSTPGRLNQTSMFINRPGIYFGQCSEICGINHSFMPIAVEST 213
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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